SitesBLAST
Comparing BWI76_RS13195 FitnessBrowser__Koxy:BWI76_RS13195 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
4xgiA Crystal structure of glutamate dehydrogenase from burkholderia thailandensis
63% identity, 99% coverage: 5:423/424 of query aligns to 4:416/416 of 4xgiA
- active site: K112 (= K113), D152 (= D153)
- binding 2-oxoglutaric acid: K76 (= K77), G78 (= G79), M97 (= M98), K100 (= K101), K112 (= K113), A150 (= A151), R192 (= R193), S355 (= S356)
- binding nicotinamide-adenine-dinucleotide: R80 (= R81), D152 (= D153), V153 (= V154), T196 (= T197), G224 (= G225), G226 (= G227), N227 (= N228), V228 (= V229), D248 (= D249), H249 (= H250), A299 (= A300), A300 (= A301), A322 (= A323), N323 (= N324), N348 (= N349)
3aoeB Crystal structure of hetero-hexameric glutamate dehydrogenase from thermus thermophilus (leu bound form)
61% identity, 100% coverage: 2:423/424 of query aligns to 4:424/424 of 3aoeB
3aogA Crystal structure of glutamate dehydrogenase (gdhb) from thermus thermophilus (glu bound form)
61% identity, 100% coverage: 2:423/424 of query aligns to 1:421/421 of 3aogA
- active site: K111 (= K113), D151 (= D153)
- binding glutamic acid: A70 (≠ S72), G77 (= G79), M96 (= M98), K111 (= K113), P150 (= P152), D151 (= D153), D164 (= D166), M168 (= M170), S354 (= S356), R417 (= R419), G418 (= G420), L419 (≠ I421), Y420 (= Y422)
8xd5A Cryo-em structure of glutamate dehydrogenase from thermococcus profundus in complex with NADP and glu in the steady stage of reaction
47% identity, 96% coverage: 13:420/424 of query aligns to 5:415/419 of 8xd5A
- binding gamma-l-glutamic acid: K69 (= K77), M90 (= M98), K105 (= K113), A143 (= A151), D145 (= D153), S351 (= S356)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: R73 (= R81), D145 (= D153), V146 (= V154), Y147 (≠ G155), T191 (= T197), Y220 (≠ F226), G221 (= G227), N222 (= N228), A223 (≠ V229), D244 (= D249), S245 (≠ H250), K264 (≠ Q269), N281 (≠ K286), A295 (= A300), A296 (= A301), I297 (≠ L302), N319 (= N324), N344 (= N349)
8xcsA Cryo-em structure of glutamate dehydrogenase from thermococcus profundus in complex with NADPH, akg and nh4 in the initial stage of reaction
47% identity, 96% coverage: 13:420/424 of query aligns to 4:414/418 of 8xcsA
- binding 2-oxoglutaric acid: K68 (= K77), G70 (= G79), M89 (= M98), K92 (= K101), K104 (= K113), A142 (= A151), D144 (= D153), G346 (= G352), S350 (= S356)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: R72 (= R81), K112 (≠ F121), P143 (= P152), D144 (= D153), V145 (= V154), Y146 (≠ G155), T190 (= T197), Y219 (≠ F226), G220 (= G227), N221 (= N228), A222 (≠ V229), D243 (= D249), S244 (≠ H250), K263 (≠ Q269), A295 (= A301), I296 (≠ L302), N318 (= N324)
8xcoA Cryo-em structure of glutamate dehydrogenase from thermococcus profundus incorporating NADPH in the initial stage of reaction
47% identity, 96% coverage: 13:420/424 of query aligns to 2:412/416 of 8xcoA
P28997 NAD-specific glutamate dehydrogenase; NAD-GDH; EC 1.4.1.2 from Peptoniphilus asaccharolyticus (Peptostreptococcus asaccharolyticus) (see 2 papers)
49% identity, 91% coverage: 37:422/424 of query aligns to 30:421/421 of P28997
- E243 (vs. gap) Important for nucleotide recognition; mutation to D: Shows a 9-fold relaxation of the strong discrimination against NADPH due to the decrease of binding affinity for NADH and the increase for NADPH.; mutation to K: Severely crippled in its ability to bind to NADH. Decrease of binding affinity for NADH and increase for NADPH.; mutation to R: Decrease of binding affinity for NADH and increase for NADPH.
- W244 (vs. gap) mutation to S: Decrease of binding affinity for NADH and increase for NADPH.
- D245 (vs. gap) mutation to K: Decrease of binding affinity for NADH and increase for NADPH.
P39633 Catabolic NAD-specific glutamate dehydrogenase RocG; NAD-GDH; Glutamate dehydrogenase; GlutDH; Trigger enzyme RocG; EC 1.4.1.2 from Bacillus subtilis (strain 168) (see 2 papers)
44% identity, 95% coverage: 17:420/424 of query aligns to 23:422/424 of P39633
- E27 (≠ Q21) mutation to F: Increase of thermostability 8 degrees Celsius higher than that of the wild-type.
- E93 (= E90) mutation to K: Reduces the affinity for glutamate and ammonium.
- D122 (= D119) mutation to N: Unable to control gltAB expression via an inhibitory interactions with the transcriptional regulator GltC. Reduces the affinity for glutamate and ammonium.
- Q144 (≠ I141) mutation to R: Increase of thermostability 20 degrees Celsius higher than that of the wild-type.
- Y158 (≠ G155) mutation to H: Reduces the affinity for glutamate and ammonium.
- S234 (= S231) mutation to R: Reduces the affinity for glutamate and ammonium.
- A324 (≠ G322) mutation to R: No effect.
6yeiA Arabidopsis thaliana glutamate dehydrogenase isoform 1 in complex with NAD (see paper)
46% identity, 95% coverage: 20:420/424 of query aligns to 8:407/409 of 6yeiA
- binding potassium ion: S26 (≠ T38), L27 (= L39), I29 (≠ H41), P30 (= P42)
- binding nicotinamide-adenine-dinucleotide: T184 (= T197), F213 (= F226), G214 (= G227), N215 (= N228), V216 (= V229), D236 (= D249), I237 (≠ H250), A288 (= A301), L289 (= L302), A310 (= A323), N311 (= N324), N336 (= N349)
6yehA Arabidopsis thaliana glutamate dehydrogenase isoform 1 in apo form (see paper)
46% identity, 95% coverage: 20:420/424 of query aligns to 8:407/410 of 6yehA
6yeiF Arabidopsis thaliana glutamate dehydrogenase isoform 1 in complex with NAD (see paper)
46% identity, 95% coverage: 20:420/424 of query aligns to 9:408/410 of 6yeiF
- binding 2-oxoglutaric acid: K66 (= K77), G68 (= G79), M87 (= M98), K90 (= K101), K102 (= K113), A140 (= A151), V341 (= V353), S344 (= S356)
- binding potassium ion: S27 (≠ T38), L28 (= L39), I30 (≠ H41), P31 (= P42), F32 (≠ K43)
- binding nicotinamide-adenine-dinucleotide: R70 (= R81), D142 (= D153), M143 (≠ V154), T185 (= T197), F214 (= F226), G215 (= G227), N216 (= N228), V217 (= V229), D237 (= D249), I238 (≠ H250), A288 (= A300), A289 (= A301), A311 (= A323), N312 (= N324), N337 (= N349)
P50735 Cryptic catabolic NAD-specific glutamate dehydrogenase GudB; NAD-GDH; EC 1.4.1.2 from Bacillus subtilis (strain 168) (see paper)
47% identity, 91% coverage: 37:420/424 of query aligns to 40:425/427 of P50735
- VKA 97:99 (≠ VMA 91:93) mutation Missing: In gudB1; gains glutamate dehydrogenase activity, restores growth on proline, arginine, ornithine.
8owmC Crystal structure of glutamate dehydrogenase 2 from arabidopsis thaliana binding ca, NAD and 2,2-dihydroxyglutarate (see paper)
45% identity, 90% coverage: 38:420/424 of query aligns to 29:410/413 of 8owmC
- binding calcium ion: S29 (≠ T38), I32 (≠ H41)
- binding nicotinamide-adenine-dinucleotide: D144 (= D153), M145 (≠ V154), R183 (= R193), T187 (= T197), F216 (= F226), G217 (= G227), N218 (= N228), V219 (= V229), D239 (= D249), I240 (≠ H250), C290 (≠ A300), A291 (= A301), A313 (= A323), N314 (= N324), N339 (= N349)
- binding 2,2-bis(oxidanyl)pentanedioic acid: K68 (= K77), G70 (= G79), M89 (= M98), K92 (= K101), K104 (= K113), A142 (= A151), R183 (= R193), N314 (= N324), V343 (= V353), S346 (= S356)
1v9lA L-glutamate dehydrogenase from pyrobaculum islandicum complexed with NAD (see paper)
44% identity, 91% coverage: 37:420/424 of query aligns to 26:416/418 of 1v9lA
- active site: K102 (= K113), D142 (= D153)
- binding nicotinamide-adenine-dinucleotide: T186 (= T197), Q213 (= Q224), G216 (= G227), N217 (= N228), V218 (= V229), D238 (= D249), I239 (≠ H250), A296 (= A301), I297 (≠ L302), A318 (= A323), N319 (= N324), N344 (= N349)
3aoeF Crystal structure of hetero-hexameric glutamate dehydrogenase from thermus thermophilus (leu bound form)
42% identity, 99% coverage: 5:423/424 of query aligns to 3:417/417 of 3aoeF
P80053 Glutamate dehydrogenase 2; GDH-2; EC 1.4.1.3 from Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) (Sulfolobus solfataricus) (see paper)
41% identity, 97% coverage: 11:421/424 of query aligns to 7:419/420 of P80053
- K254 (≠ G258) modified: N6-methyllysine
- K260 (≠ A264) modified: N6-methyllysine
- K372 (≠ A376) modified: N6-methyllysine
- K391 (≠ E395) modified: N6-methyllysine
- K392 (= K396) modified: N6-methyllysine
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylmethionine
8ar7A Bovine glutamate dehydrogenase in ternary complex with the allosteric activators adp and leucine (see paper)
44% identity, 75% coverage: 46:364/424 of query aligns to 55:385/496 of 8ar7A
Sites not aligning to the query:
- binding adenosine-5'-diphosphate: 389, 392, 455, 484, 488
- binding potassium ion: 47, 48, 49, 50, 51, 52
- binding leucine: 493, 494, 495
6dhlA Bovine glutamate dehydrogenase complexed with epicatechin-3-gallate (ecg) (see paper)
44% identity, 75% coverage: 46:364/424 of query aligns to 54:384/496 of 6dhlA
- binding (2R,3S)-2-(3,4-dihydroxyphenyl)-5,7-dihydroxy-3,4-dihydro-2H-chromen-3-yl 3,4,5-trihydroxybenzoate: H80 (≠ S72), R81 (= R73), C110 (= C102), D114 (≠ N106), V115 (≠ I107), K382 (≠ Q362)
Sites not aligning to the query:
6dhdA Bovine glutamate dehydrogenase complexed with nadh, gtp, glutamate (see paper)
44% identity, 75% coverage: 46:364/424 of query aligns to 59:389/501 of 6dhdA
- active site: K126 (= K113), D168 (= D153)
- binding glutamic acid: K90 (= K77), M111 (= M98), K114 (= K101), K126 (= K113), A166 (= A151), V378 (= V353), S381 (= S356)
- binding guanosine-5'-triphosphate: H209 (≠ L191), S213 (≠ K195), R217 (= R199), H258 (≠ E232), R261 (= R235), Y262 (≠ L236), R265 (≠ G239), E292 (≠ T266)
- binding 1,4-dihydronicotinamide adenine dinucleotide: H85 (≠ S72), R86 (= R73), R94 (= R81), A116 (= A103), D119 (≠ N106), V120 (≠ I107), D168 (= D153), M169 (≠ V154), H195 (≠ T177), Q205 (≠ L187), G206 (= G188), T215 (= T197), Q250 (= Q224), F252 (= F226), G253 (= G227), N254 (= N228), V255 (= V229), E275 (≠ D249), S276 (≠ H250), A326 (= A301), A348 (= A323), N349 (= N324), N374 (= N349), K387 (≠ Q362), N388 (≠ D363)
Sites not aligning to the query:
3etgA Glutamate dehydrogenase complexed with gw5074 (see paper)
44% identity, 75% coverage: 46:364/424 of query aligns to 59:389/501 of 3etgA
- active site: K126 (= K113), D168 (= D153)
- binding glutamic acid: K90 (= K77), M111 (= M98), K114 (= K101), A166 (= A151), V378 (= V353), S381 (= S356)
- binding guanosine-5'-triphosphate: H209 (≠ L191), G210 (= G192), S213 (≠ K195), R217 (= R199), R261 (= R235), R265 (≠ G239), E292 (≠ T266)
- binding (3E)-3-[(3,5-dibromo-4-hydroxyphenyl)methylidene]-5-iodo-1,3-dihydro-2H-indol-2-one: R146 (= R133), R147 (= R134), M150 (≠ S137)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: D168 (= D153), M169 (≠ V154), R211 (= R193), T215 (= T197), Q250 (= Q224), G253 (= G227), V255 (= V229), E275 (≠ D249), S276 (≠ H250), A326 (= A301), G347 (= G322), A348 (= A323), N349 (= N324), N374 (= N349)
Query Sequence
>BWI76_RS13195 FitnessBrowser__Koxy:BWI76_RS13195
MEKLSYASESSTSPWTTYLRQIDRVAPYLGDLAFWIETLRHPKRALIVDIPVQMDDGTIR
HFEGYRVQHNLSRGPGKGGVRYHPDVDLNEVMALSAWMTIKCAAVNIPYGGAKGGIRVDP
FSLSEGELERLTRRYTSEIGIIIGPQKDIPAPDVGTNGKVMAWMMDTYSMNHGTTITGVV
TGKPIHLGGSLGREKATGRGVFVTGREVARRSGIEIEGAKVALQGFGNVGSEAARLFAGV
GARIVVIQDHTATLYNEGGIDMAALTAWQAENKQIAGFPGAREIAKEAFWTTPMDILIPA
ALEGQITRERAETLSCKLVLEGANGPTYPEADDVLAERGIVVVPDVICNAGGVTVSYFEW
VQDMASFFWSEEEINAKMDRIMTDAIVHVYEKAVEKACSLRTAAYIVACERILMARKDRG
IYPG
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SitesBLAST's Database
SitesBLAST's database includes
(1) SwissProt
entries with experimentally-supported functional features;
and (2) protein structures with bound ligands, from the
BioLip database.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory